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A sliding clamp monkey wrench

Nature Structural Biology volume 8, pages829–831(2001)Cite this article

Crystal structures of the Escherichia coli DNA replication γ clamp loading complex and of a subunit of the clamp loader bound to a β clamp monomer provide a physical framework in which to view ATP-dependent modulation of γ complex–β interactions. The structural data suggest how the β ring is opened and loaded onto DNA in the absence of a direct interaction between the γ complex and the β dimer interface.

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Figure 1: Schematic diagram of the E. coli replisome containing a dimeric polymerase capable of coordinated leading and lagging strand synthesis.
Figure 2: Ribbon diagrams based on crystal structures of sliding clamps from a, E. coli (β)3, b, humans (PCNA)5, and c, bacteriophage T4 (gp45)6.
Figure 3: Schematic diagram of the δ–β interaction that results in clamp opening.
Figure 4: Schematic diagram of the ATP-induced conformational change in the E. coli clamp loader2.

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Affiliations

  1. the Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, 32610-0245, Florida, USA

    Linda B. Bloom

  2. the Department of Biological Sciences, Hedco Laboratories, University of Southern California, Los Angeles, 90089-1340, Calfornia, USA

    Myron F. Goodman

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  1. Linda B. Bloom
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  2. Myron F. Goodman
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Correspondence to Linda B. Bloom.

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Bloom, L., Goodman, M. A sliding clamp monkey wrench. Nat Struct Mol Biol 8, 829–831 (2001). https://doi.org/10.1038/nsb1001-829

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